Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9P996 (PSB_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit beta

EC=3.4.25.1
Alternative name(s):
20S proteasome beta subunit
Proteasome core protein PsmB
Gene names
Name:psmB
Ordered Locus Names:AF_0481
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation By similarity. HAMAP-Rule MF_02113

Catalytic activity

Cleavage of peptide bonds with very broad specificity. HAMAP-Rule MF_02113

Enzyme regulation

The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity By similarity. HAMAP-Rule MF_02113

Subunit structure

The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has probably a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is likely capped at one or both ends by the proteasome regulatory ATPase, PAN. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02113.

Sequence similarities

Belongs to the peptidase T1B family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1111Removed in mature form; by autocatalysis By similarity
PRO_0000026659
Chain12 – 213202Proteasome subunit beta HAMAP-Rule MF_02113
PRO_0000026660

Sites

Active site121Nucleophile By similarity

Secondary structure

................................... 213
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9P996 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: DA03E480A88F8227

FASTA21323,418
        10         20         30         40         50         60 
MSMIEEKIYK GTTTVGLVCK DGVVMATEKR ATMGNFIASK AAKKIYQIAD RMAMTTAGSV 

        70         80         90        100        110        120 
GDAQFLARII KIEANLYEIR RERKPTVRAI ATLTSNLLNS YRYFPYLVQL LIGGIDSEGK 

       130        140        150        160        170        180 
SIYSIDPIGG AIEEKDIVAT GSGSLTAYGV LEDRFTPEIG VDEAVELAVR AIYSAMKRDS 

       190        200        210 
ASGDGIDVVK ITEDEFYQYS PEEVEQILAK FRK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000782 Genomic DNA. Translation: AAB90757.1.
PIRA69310.
RefSeqNP_069317.1. NC_000917.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2QX-ray2.83H/I/J/K/L/M/N12-213[»]
ProteinModelPortalQ9P996.
SMRQ9P996. Positions 12-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9P996. 1 interaction.
STRING224325.AF0481.

Protein family/group databases

MEROPST01.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB90757; AAB90757; AF_0481.
GeneID1483698.
KEGGafu:AF0481.

Phylogenomic databases

eggNOGCOG0638.
KOK03433.
OMAMVDWLGT.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-494-MONOMER.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
HAMAPMF_02113_A. Proteasome_B_A.
InterProIPR029055. Ntn_hydrolases_N.
IPR019983. Pept_T1A_Psome_bsu_arc.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR03634. arc_protsome_B. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9P996.

Entry information

Entry namePSB_ARCFU
AccessionPrimary (citable) accession number: Q9P996
Secondary accession number(s): O29769
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references